Emulsifying and structural properties of .BETA.-lactoglobulin at different pHs.

• SHIMIZU Makoto

  Department of Agricultural Chemistry, The University of Tokyo

• SAITO Masayoshi

  Department of Agricultural Chemistry, The University of Tokyo

• YAMAUCHI Kunio

  Department of Agricultural Chemistry, The University of Tokyo

抄録

The emulsifying properties of β-lactoglobulin (β-Lg) in relation to its molecular structure were investigated at pH 3-9. In the acidic pH region, β-Lg showed relatively low emulsifying and surface activity, while its surface hydrophobicity was greater than at neutral pHs. The conformational stability of β-Lg varied depending on pH, i.e. its conformation was more rigid and resistant to denaturation at pH 3 than at pH 7. The low emulsifying and surface activity of β-Lg at acidic pHs was assumed to be due to such low denaturability (flexibility) of the molecule. Cleavage of the intramolecular disulfide bonds increased the denaturability, as well as the emulsifying activity, of β-Lg at pH 3.

収録刊行物

• Agricultural and Biological Chemistry

  Agricultural and Biological Chemistry 49 (1), 189-194, 1985

  公益社団法人 日本農芸化学会

キーワード

• General Agricultural and Biological Sciences
• General Biochemistry, Genetics and Molecular Biology

詳細情報

• CRID: 1390001206467420288
• NII論文ID: 130000026680
• DOI: 10.1271/bbb1961.49.189
• COI: 1:CAS:528:DyaL2MXhtFWksr8%3D
• ISSN: 18811280
• ISSN: 00021369
• ISSN: http://id.crossref.org/issn/00021369
• 本文言語コード: en
• データソース種別:
  • JaLC
  • Crossref
  • CiNii Articles
• 抄録ライセンスフラグ: 使用不可